MolNFT v1 · #147903 · protein
X-ray structure of trypanothione reductase from leishmania infantum in complex with 2-(DIETHYLAMINO)ETHYL 4-((3-(4-nitrophenyl)-3- OXOPROPYL)AMINO)BENZOATE
6ER5: “X-ray structure of trypanothione reductase from leishmania infantum in complex with 2-(DIETHYLAMINO)ETHYL…”. X-ray diffraction, 3 ligands (FAD, BVN, SO4). MolNFT v1 #147903 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6ER5
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A4HSF7
- Ligands
- FAD, BVN, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 488 | — | A4HSF7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- BVN · 2-(diethylamino)ethyl 4-((3-(4-nitrophenyl)-3-oxopropyl)amino)benzoate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ER5 · X-ray structure of Trypanothione Reductase from Leishmania infantum in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A4HSF7
- Elsewhere: RCSB PDB 6ER5 · PDBe 6ER5 · UniProt A4HSF7
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